Structure and expression of human dihydropteridine reductase

J Lockyer; R G Cook; S Milstein; S Kaufman; S L. C. Woo; Fred Ledley; S Milstien

doi:0027-8424

Structure and expression of human dihydropteridine reductase

J Lockyer
, R G Cook
, S Milstein
, S Kaufman
, S L. C. Woo
, Fred Ledley
, S Milstien

Natural and Applied Sciences

Research output: Contribution to journal › Article

Abstract

Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. A cDNA for human DHPR was isolated from a human liver cDNA library in the vector lambda gt11 using a monospecific antibody against sheep DHPR. The nucleic acid sequence and amino acid sequence of human DHPR were determined from a full-length clone. A 112 amino acid sequence of sheep DHPR was obtained by sequencing purified sheep DHPR. This sequence is highly homologous to the predicted amino acid sequence of the human protein. Gene transfer of the recombinant human DHPR into COS cells leads to expression of DHPR enzymatic activity. These results indicate that the cDNA clone identified by antibody screening is an authentic and full-length cDNA for human DHPR.

Original language	English
Pages (from-to)	3329-3333
Journal	Proceedings of the National Academy of Sciences (PNAS)
Volume	84
Issue number	84
DOIs	https://doi.org/0027-8424
State	Published - 1987

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@article{1f9f1c623f2746448abdbfa650a86610,

title = "Structure and expression of human dihydropteridine reductase",

abstract = "Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. A cDNA for human DHPR was isolated from a human liver cDNA library in the vector lambda gt11 using a monospecific antibody against sheep DHPR. The nucleic acid sequence and amino acid sequence of human DHPR were determined from a full-length clone. A 112 amino acid sequence of sheep DHPR was obtained by sequencing purified sheep DHPR. This sequence is highly homologous to the predicted amino acid sequence of the human protein. Gene transfer of the recombinant human DHPR into COS cells leads to expression of DHPR enzymatic activity. These results indicate that the cDNA clone identified by antibody screening is an authentic and full-length cDNA for human DHPR.",

author = "J Lockyer and Cook, \{R G\} and S Milstein and S Kaufman and Woo, \{S L. C.\} and Fred Ledley and S Milstien",

year = "1987",

doi = "0027-8424",

language = "English",

volume = "84",

pages = "3329--3333",

journal = "Proceedings of the National Academy of Sciences (PNAS)",

number = "84",

}

TY - JOUR

T1 - Structure and expression of human dihydropteridine reductase

AU - Lockyer, J

AU - Cook, R G

AU - Milstein, S

AU - Kaufman, S

AU - Woo, S L. C.

AU - Ledley, Fred

AU - Milstien, S

PY - 1987

Y1 - 1987

N2 - Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. A cDNA for human DHPR was isolated from a human liver cDNA library in the vector lambda gt11 using a monospecific antibody against sheep DHPR. The nucleic acid sequence and amino acid sequence of human DHPR were determined from a full-length clone. A 112 amino acid sequence of sheep DHPR was obtained by sequencing purified sheep DHPR. This sequence is highly homologous to the predicted amino acid sequence of the human protein. Gene transfer of the recombinant human DHPR into COS cells leads to expression of DHPR enzymatic activity. These results indicate that the cDNA clone identified by antibody screening is an authentic and full-length cDNA for human DHPR.

AB - Dihydropteridine reductase (DHPR; EC 1.6.99.7) catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin and is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. A cDNA for human DHPR was isolated from a human liver cDNA library in the vector lambda gt11 using a monospecific antibody against sheep DHPR. The nucleic acid sequence and amino acid sequence of human DHPR were determined from a full-length clone. A 112 amino acid sequence of sheep DHPR was obtained by sequencing purified sheep DHPR. This sequence is highly homologous to the predicted amino acid sequence of the human protein. Gene transfer of the recombinant human DHPR into COS cells leads to expression of DHPR enzymatic activity. These results indicate that the cDNA clone identified by antibody screening is an authentic and full-length cDNA for human DHPR.

U2 - 0027-8424

DO - 0027-8424

M3 - Article

VL - 84

SP - 3329

EP - 3333

JO - Proceedings of the National Academy of Sciences (PNAS)

JF - Proceedings of the National Academy of Sciences (PNAS)

IS - 84

ER -

Structure and expression of human dihydropteridine reductase

Abstract

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